Crystal structure of FGF1 complexed with the ectodomain of FGFR2b harboring the A172F Pfeiffer syndrome mutation. Determined by X-ray diffraction at 2.2 Å resolution. Released 31 Aug 2011.
Explore 3OJ2 in 3D Show helices and sheets RCSB PDB PDBe
3OJ2 contains 22 α-helices and 70 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-24 | 3 | |
| β-strand | 27-31 | 5 | 1 |
| β-strand | 37-40 | 4 | 1 |
| β-strand | 45-49 | 5 | 1 |
| β-strand | 59-65 | 7 | 1 |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 79-82 | 4 | 1 |
| β-strand | 88-91 | 4 | 1 |
| β-strand | 100-104 | 5 | 1 |
| β-strand | 110-114 | 5 | 1 |
| α-helix | 118-120 | 3 | |
| β-strand | 123 | 1 | 1 |
| β-strand | 126 | 1 | 2 |
| β-strand | 131 | 1 | 1 |
| β-strand | 132 | 1 | 2 |
| α-helix | 135-137 | 3 | |
| α-helix | 143-145 | 3 | |
| β-strand | 147-150 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 152-156 | 5 | 5 |
| α-helix | 159-162 | 4 | |
| β-strand | 166-170 | 5 | 6 |
| β-strand | 175-178 | 4 | 7 |
| β-strand | 181-184 | 4 | 5 |
| α-helix | 186-187 | 2 | |
| β-strand | 188-193 | 6 | 6 |
| β-strand | 196-197 | 2 | 6 |
| α-helix | 200-202 | 3 | |
| β-strand | 208-210 | 3 | 7 |
| β-strand | 215-218 | 4 | 7 |
| α-helix | 223-225 | 3 | |
| β-strand | 227-235 | 9 | 6 |
| β-strand | 238-249 | 12 | 6 |
| β-strand | 257-258 | 2 | 8 |
| α-helix | 259 | 1 | |
| β-strand | 266-269 | 4 | 9 |
| β-strand | 274-277 | 4 | 10 |
| β-strand | 280-281 | 2 | 8 |
| α-helix | 285-286 | 2 | |
| β-strand | 287-294 | 8 | 9 |
| β-strand | 301 | 1 | 11 |
| α-helix | 306 | 1 | |
| β-strand | 307 | 1 | 11 |
| β-strand | 308-314 | 7 | 9 |
| β-strand | 324-327 | 4 | 10 |
| β-strand | 336-343 | 8 | 9 |
| β-strand | 348-358 | 11 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heparin-binding growth factor 1 | A, B | protein | 155 | Homo sapiens | P05230 (AlphaFold model) |
| Fibroblast growth factor receptor 2 | C, D | protein | 231 | Homo sapiens | P21802 (AlphaFold model) |
>3OJ2_1 Heparin-binding growth factor 1 (chains A, B) MAEGEITTFTALTEKFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQ LSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEK NWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD
>3OJ2_2 Fibroblast growth factor receptor 2 (chains C, D) MAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAFNTVKFRCPAGGNPMPTMRWLKNGKEF KQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPIL QAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKHSGIN SSNAEVLALFNVTEADAGEYICKVSNYIGQANQSAWLTVLPKQQAPGREKE
Plasticity in Interactions of Fibroblast Growth Factor 1 (FGF1) N Terminus with FGF Receptors Underlies Promiscuity of FGF1. Beenken, A., Eliseenkova, A.V., Ibrahimi, O.A. et al. J Biol Chem (2012) 287:3067-3078. DOI 10.1074/jbc.M111.275891 · PubMed
Other PDB entries of the same protein (UniProt P05230 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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